ID   A0A080N2Y0_9BIFI        Unreviewed;      1003 AA.
AC   A0A080N2Y0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glycosyl hydrolase family 38 protein, alpha-mannosidase {ECO:0000313|EMBL:KFF31428.1};
DE            EC=3.2.1.24 {ECO:0000313|EMBL:KFF31428.1};
GN   ORFNames=BBOMB_0781 {ECO:0000313|EMBL:KFF31428.1};
OS   Bifidobacterium bombi DSM 19703.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1341695 {ECO:0000313|EMBL:KFF31428.1, ECO:0000313|Proteomes:UP000028730};
RN   [1] {ECO:0000313|EMBL:KFF31428.1, ECO:0000313|Proteomes:UP000028730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19703 {ECO:0000313|EMBL:KFF31428.1,
RC   ECO:0000313|Proteomes:UP000028730};
RX   PubMed=25085493; DOI=10.1128/AEM.02308-14;
RA   Milani C., Lugli G.A., Duranti S., Turroni F., Bottacini F., Mangifesta M.,
RA   Sanchez B., Viappiani A., Mancabelli L., Taminiau B., Delcenserie V.,
RA   Barrangou R., Margolles A., van Sinderen D., Ventura M.;
RT   "Genomic encyclopedia of type strains of the genus Bifidobacterium.";
RL   Appl. Environ. Microbiol. 80:6290-6302(2014).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFF31428.1}.
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DR   EMBL; ATLK01000001; KFF31428.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A080N2Y0; -.
DR   STRING; 1341695.BBOMB_0781; -.
DR   eggNOG; COG0383; Bacteria.
DR   Proteomes; UP000028730; Unassembled WGS sequence.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR   CDD; cd10789; GH38N_AMII_ER_cytosolic; 1.
DR   Gene3D; 2.60.40.2220; -; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR041147; GH38_C.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR011682; Glyco_hydro_38_C.
DR   InterPro; IPR015341; Glyco_hydro_38_cen.
DR   InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR   InterPro; IPR000602; Glyco_hydro_38_N.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR   PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF17677; Glyco_hydro38C2; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000313|EMBL:KFF31428.1};
KW   Hydrolase {ECO:0000313|EMBL:KFF31428.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028730}.
FT   DOMAIN          519..597
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1003 AA;  112159 MW;  E9BE2DCDFDE0808D CRC64;
     MNVSTASEKT KKRAERMLTQ YLPNALYKRT SPVCIESWKV GGEPVSFETA KNAQYKPIQV
     GAAWGAPWDT WWFHITGTVP DFWNEEETQP ELVVDLGVNG SGPGFQAEAL VYDADGTVIK
     AIEPYNGSVR LPHPGGSFEW YIEAAANPDI ASRAKTAGTP LGDEGVQDGP ELYELRRLEM
     GQLDLEVWNL IQELTVLSGL CDEIDKDRTR YAQILSAIDE ALNLINIDDP GLTVHSARAI
     LAKQLAKPAV EGHTVYAVGH AHIDSAWLWP LRETRRKVAR TFSNVVNLTD QDRELVFAAS
     SAQQYQWLKE DHPQLFKEVQ RKAADGQFIP VGGMWVESDA NLPGGESLAR QFLQGTQFFR
     RHFDNMAPIA WLPDSFGYSA SFPQIARLSG IQYFLTQKIS WNDTNVFPHH SFLWQGLDGT
     QIFTHFPPSD TYNACVSPYE VALSEKQYSE KGKGTSSLML FGWGDGGGGP TREMMAAARL
     QHNLEGSPKL TVTNPMEFFE QASKEMSCPP VWRGELYLEL HRGTGTSHAQ TKQGNRRCEA
     LLHEAELWAT YASVLTGKEY PLSTFDDIWH KVLLYQFHDI LPGSAISWVY AEVERSQAEI
     MEKLETMIKE SLQALVGTGT KSLIANAAPL HQRHTPAGAI VQSTETETWG SAKRKGDHVV
     LENDNVSYEI DTEGHIVSAY DKNNKRENID PAMPGNVLQL FEDAPTNWDA WDIDSTYEGM
     EQPAAIVDGI DIGADQVTVS GTIGRSKYAQ HVRLDNDTNM LHIHTHINWN ESNHLLKQAF
     PTNIYATEAT CEVQFGHLTR PVVKNTSWDE AKFESASQRW VHIADGDFGV SIANRSTYAY
     DFRQIKLSND RPGTQIRASL LRSPHYPDPR QDLGEHDFDI AFGVGSTIPD AIRAGYRINL
     PARAMEGEHE IEPLLTVDNP NVILESLKMS QDGSNAVIAR FYESSGGTSR THLDINFSYN
     DIKEVGILEE VCEAVQPVIR TMEASHLELE LHPFQIVTLR FER
//